SinR
- Description: transcriptional regulator of post-exponential-phase responses genes
Gene name | sinR |
Synonyms | sin, flaD |
Essential | no |
Product | transcriptional regulator of post-exponential-phase responses genes |
Function | control of biofilm formation |
Interactions involving this protein in SubtInteract: SinR | |
Metabolic function and regulation of this protein in SubtiPathways: Biofilm, Central C-metabolism, Protein secretion | |
MW, pI | 12 kDa, 7.177 |
Gene length, protein length | 333 bp, 111 aa |
Immediate neighbours | sinI, tasA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
transcription factors and their control, transition state regulators, biofilm formation
This gene is a member of the following regulons
AbrB regulon, ScoC regulon, Spo0A regulon
The SinR regulon
The gene
Basic information
- Locus tag: BSU24610
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: transcription repressor of biofilm genes, acts as co-repressor for SlrR PubMed
- Protein family:
- Paralogous protein(s): SlrR
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P06533
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant: TMB079 sinR::spec, GP736 (tetR), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Modelling of the SinI/SinR switch
Original publications
Additonal publications: PubMed
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947